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P22811

- XDH_DROPS

UniProt

P22811 - XDH_DROPS

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Protein

Xanthine dehydrogenase

Gene

ry

Organism
Drosophila pseudoobscura pseudoobscura (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid (By similarity).By similarity

Catalytic activityi

Xanthine + NAD+ + H2O = urate + NADH.
Hypoxanthine + NAD+ + H2O = xanthine + NADH.

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters.By similarity
  • FADBy similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Iron-sulfur 1By similarity
Metal bindingi52 – 521Iron-sulfur 1By similarity
Metal bindingi55 – 551Iron-sulfur 1By similarity
Metal bindingi77 – 771Iron-sulfur 1By similarity
Metal bindingi117 – 1171Iron-sulfur 2By similarity
Metal bindingi120 – 1201Iron-sulfur 2By similarity
Metal bindingi152 – 1521Iron-sulfur 2By similarity
Metal bindingi154 – 1541Iron-sulfur 2By similarity
Binding sitei343 – 3431FADBy similarity
Binding sitei366 – 3661FADBy similarity
Binding sitei414 – 4141FAD; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei432 – 4321FADBy similarity
Metal bindingi780 – 7801MolybdenumBy similarity
Metal bindingi811 – 8111Molybdenum; via carbonyl oxygenBy similarity
Binding sitei815 – 8151SubstrateBy similarity
Binding sitei893 – 8931SubstrateBy similarity
Metal bindingi925 – 9251Molybdenum; via amide nitrogenBy similarity
Binding sitei927 – 9271SubstrateBy similarity
Metal bindingi1092 – 10921Molybdenum; via amide nitrogenBy similarity
Active sitei1275 – 12751Proton acceptorBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi263 – 2708FADBy similarity
Nucleotide bindingi353 – 3575FADBy similarity

GO - Molecular functioni

  1. 2 iron, 2 sulfur cluster binding Source: UniProtKB
  2. electron carrier activity Source: InterPro
  3. flavin adenine dinucleotide binding Source: UniProtKB
  4. iron ion binding Source: InterPro
  5. molybdopterin cofactor binding Source: UniProtKB
  6. UDP-N-acetylmuramate dehydrogenase activity Source: InterPro
  7. xanthine dehydrogenase activity Source: UniProtKB
  8. xanthine oxidase activity Source: InterPro

GO - Biological processi

  1. xanthine catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Xanthine dehydrogenase (EC:1.17.1.4)
Short name:
XD
Alternative name(s):
Protein rosy locus
Gene namesi
Name:ry
Synonyms:XDH
ORF Names:GA20500
OrganismiDrosophila pseudoobscura pseudoobscura (Fruit fly)
Taxonomic identifieri46245 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000001819: Chromosome 2, UP000001819: Partially assembled WGS sequence

Organism-specific databases

FlyBaseiFBgn0012736. Dpse\ry.

Subcellular locationi

Peroxisome By similarity

GO - Cellular componenti

  1. peroxisome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13431343Xanthine dehydrogenasePRO_0000166080Add
BLAST

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi7237.FBpp0282224.

Structurei

3D structure databases

ProteinModelPortaliP22811.
SMRiP22811. Positions 9-169.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 95882Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini235 – 424190FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG4630.
InParanoidiP22811.
KOiK00106.
OrthoDBiEOG7QRQSZ.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
IPR014307. Xanthine_DH_ssu.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsiTIGR02963. xanthine_xdhA. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22811-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSGQQKTSEL VFFVNGKKVT DTNPDPECTL LTYLRDKLRL CGTKLGCAEG
60 70 80 90 100
GCGACTVVIS RMDRGQNKIR HLAVNACLTP VCAMHGCAVT TVEGIGSTRT
110 120 130 140 150
RLHPVQERLA KAHGSQCGFC TPGIVMSMYA LLRSAEQPSM RDLEVAFQGN
160 170 180 190 200
LCRCTGYRPI LEGYKTFTKE FACGMGDKCC KVNGKGCGGG DDTQSVTDDT
210 220 230 240 250
LFERSQFQPL DPSQEPIFPP ELQLTPTYDS ESLIFSSERV TWYRPTTLQE
260 270 280 290 300
LLQLKSDHPS AKLVVGNTEV GVEVKFKHFL YPHLINPTQV PELLEVRESE
310 320 330 340 350
ESIYFGAAVS LMEIDALLRQ RIEELPEAQT RLFQCAVDML HYFAGKQIRN
360 370 380 390 400
VACLGGNIMT GSPISDMNPV LTAAGARLEV ASLVGGKTSH RTVHMGTGFF
410 420 430 440 450
TGYRRNVIEP HEVLLGIHFQ KTTPDQHVVA FKQARRRDDD IAIVNAAVNV
460 470 480 490 500
RFEPRTNVVA GISMAFGGMA PTTVLAPRTS QLMVKQPLDH HLVERVAESL
510 520 530 540 550
CGELPLAASA PGGMIAYRRA LVVSLIFKAY LSISRKLSEA GIISTDAIPA
560 570 580 590 600
EERSGAELFH TPVLRSAQLF ERVCSEQPVC DPIGRPEVHA AALKQATGEA
610 620 630 640 650
IYTDDIPRMD GELYLGLVLS TKPRAKITKL DASEALALEG VHAFFSHKDL
660 670 680 690 700
TEHENEVGPV FHDEHVFAAA EVHCYGQIVG AVAADNKALA QRAARLVRVE
710 720 730 740 750
YEELAPVIVT IEQAIEHGSY FPDYPRYVNK GNVEEAFAAA EHTYEGSCRM
760 770 780 790 800
GGQEHFYLET HAAVAVPRDS DELELFCSTQ HPSEVQKLVA HVTTLPAHRV
810 820 830 840 850
VCRAKRLGGG FGGKESRGIS VALPVALAAY RLRRPVRCML DRDEDMLITG
860 870 880 890 900
TRHPFLFKYK VAFASDGLIT ACDIECYNNA GWSMDLSFSV LERAMYHFEN
910 920 930 940 950
CYRIPNVRVG GWVCKTNLPS NTAFRGFGGP QGMFAGEHII RDVARIVGRD
960 970 980 990 1000
VLDVMRLNFY KTGDITHYNQ KLEHFPIERC LDDCLAQSRY HEKRTEIAKF
1010 1020 1030 1040 1050
NRENRWRKRG MAVIPTKYGI AFGVMHLNQA GALINVYGDG SVLLSHGGVE
1060 1070 1080 1090 1100
IGQGLNTKMI QCAARALGIP IELIHISETA TDKVPNTSPT AASVGSDLNG
1110 1120 1130 1140 1150
MAVLDACEKL NKRLAPIKEA LPQGTWQEWI NKAYFDRVSL SATGFYAMPG
1160 1170 1180 1190 1200
IGYHPETNPN ARTYSYYTNG VGISVVEIDC LTGDHQVLST DIVMDIGSSI
1210 1220 1230 1240 1250
NPAIDIGQIE GAFMQGYGLF TLEELMYSPQ GMLYSRGPGM YKLPGFADIP
1260 1270 1280 1290 1300
GEFNVSLLTG APNPRAVYSS KAVGEPPLFI GSSAFFAIKE AIAAARQEQG
1310 1320 1330 1340
LTGDFPLEAP STSARIRMAC QDKFTNLLEI PEEGSFTPWN IVP
Length:1,343
Mass (Da):147,349
Last modified:July 11, 2006 - v2
Checksum:iA58C142336E14BC9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti58 – 581V → M in AAA29022. (PubMed:2493563)Curated
Sequence conflicti200 – 2001T → A in AAA29022. (PubMed:2493563)Curated
Sequence conflicti428 – 4281V → I in AAA29022. (PubMed:2493563)Curated
Sequence conflicti428 – 4281V → I in AAX13180. (PubMed:15545653)Curated
Sequence conflicti461 – 4611G → E in AAA29022. (PubMed:2493563)Curated
Sequence conflicti461 – 4611G → E in AAX13180. (PubMed:15545653)Curated
Sequence conflicti475 – 4751L → V in AAA29022. (PubMed:2493563)Curated
Sequence conflicti734 – 7341E → D in AAX13180. (PubMed:15545653)Curated
Sequence conflicti747 – 7471S → N in AAA29022. (PubMed:2493563)Curated
Sequence conflicti762 – 7621A → G in AAA29022. (PubMed:2493563)Curated
Sequence conflicti986 – 9861A → V in AAX13180. (PubMed:15545653)Curated
Sequence conflicti1245 – 12451Missing in AAA29022. (PubMed:2493563)Curated
Sequence conflicti1320 – 13201C → F in AAA29022. (PubMed:2493563)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33977 Genomic DNA. Translation: AAA29022.1.
CM000070 Genomic DNA. Translation: EAL27642.2.
AY754605 Genomic DNA. Translation: AAX13180.1.
PIRiA31946.
RefSeqiXP_001358503.2. XM_001358466.2.

Genome annotation databases

EnsemblMetazoaiFBtr0283786; FBpp0282224; FBgn0012736.
GeneIDi4801405.
KEGGidpo:Dpse_GA20500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M33977 Genomic DNA. Translation: AAA29022.1 .
CM000070 Genomic DNA. Translation: EAL27642.2 .
AY754605 Genomic DNA. Translation: AAX13180.1 .
PIRi A31946.
RefSeqi XP_001358503.2. XM_001358466.2.

3D structure databases

ProteinModelPortali P22811.
SMRi P22811. Positions 9-169.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 7237.FBpp0282224.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0283786 ; FBpp0282224 ; FBgn0012736 .
GeneIDi 4801405.
KEGGi dpo:Dpse_GA20500.

Organism-specific databases

FlyBasei FBgn0012736. Dpse\ry.

Phylogenomic databases

eggNOGi COG4630.
InParanoidi P22811.
KOi K00106.
OrthoDBi EOG7QRQSZ.

Family and domain databases

Gene3Di 1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProi IPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
IPR022407. OxRdtase_Mopterin_BS.
IPR014307. Xanthine_DH_ssu.
[Graphical view ]
Pfami PF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000127. Xanthine_DH. 1 hit.
SMARTi SM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view ]
SUPFAMi SSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
TIGRFAMsi TIGR02963. xanthine_xdhA. 1 hit.
PROSITEi PS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
PS00559. MOLYBDOPTERIN_EUK. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of the Xdh region in Drosophila pseudoobscura and an analysis of the evolution of synonymous codons."
    Riley M.A.
    Mol. Biol. Evol. 6:33-52(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal, gene, and cis-element evolution."
    Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S., Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O., Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F., Howells S.L.
    , Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A., Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M., Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J., Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y., Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F., Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M., Weinstock G.M., Gibbs R.A.
    Genome Res. 15:1-18(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: MV2-25 / Tucson 14011-0121.94.
  3. "Patterns of selection on synonymous and nonsynonymous variants in Drosophila miranda."
    Bartolome C., Maside X., Yi S., Grant A.L., Charlesworth B.
    Genetics 169:1495-1507(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 298-1062.

Entry informationi

Entry nameiXDH_DROPS
AccessioniPrimary (citable) accession number: P22811
Secondary accession number(s): Q299Q9, Q56RA2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: July 11, 2006
Last modified: November 26, 2014
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3